Severity: Warning
Message: file_get_contents(https://...@gmail.com&api_key=61f08fa0b96a73de8c900d749fcb997acc09&a=1): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests
Filename: helpers/my_audit_helper.php
Line Number: 197
Backtrace:
File: /var/www/html/application/helpers/my_audit_helper.php
Line: 197
Function: file_get_contents
File: /var/www/html/application/helpers/my_audit_helper.php
Line: 271
Function: simplexml_load_file_from_url
File: /var/www/html/application/helpers/my_audit_helper.php
Line: 1075
Function: getPubMedXML
File: /var/www/html/application/helpers/my_audit_helper.php
Line: 3195
Function: GetPubMedArticleOutput_2016
File: /var/www/html/application/controllers/Detail.php
Line: 597
Function: pubMedSearch_Global
File: /var/www/html/application/controllers/Detail.php
Line: 511
Function: pubMedGetRelatedKeyword
File: /var/www/html/index.php
Line: 317
Function: require_once
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The impact of 1 % linseed oil or 1.08 % oleogels prepared using γ-oryzanol and β-sitosterol on the thermal aggregation behavior of myofibrillar protein (MP) was explored. The results showed that the turbidity and particle size of MP solution significantly increased after heating for 40 min. The addition of linseed oil enhanced the whiteness, turbidity and sulfhydryl content of MP, but decreased the hydrophobic interactions and disulfide bond content. When oleogels were added, the MP structure unfolded more readily during heating, and the turbidity, active sulfhydryl content and surface hydrophobicity increased by 7.80 %, 13.96 % and 60.33 % after 50 min, respectively. Oleogels reduced the fluorescence intensity of MP and contributed to the conformational transformation from α-helix to β-sheet structure. The protein aggregates in oleogels group were relatively uniform and regular in dispersion. Therefore, oleogels enhanced the unfolding of MP, and improved the thermal aggregation behavior of MP during heating.
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http://dx.doi.org/10.1016/j.foodchem.2025.144875 | DOI Listing |